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Crystal structure of the TRIM25 B30.2 (PRYSPRY) domain: a key component of antiviral signalling

Akshay A D'Cruz1, Nadia J Kershaw, Jessica J Chiang

  • 1‡Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, U.S.A.

The Biochemical Journal
|September 11, 2013
PubMed

Insights

The TRIM25 B30.2 domain structure reveals a binding pocket crucial for innate immunity. Key residues Asp488 and Trp621 are essential for TRIM25 to interact with RIG-I CARDs, enabling antiviral responses.

Area of Science:

  • Structural Biology
  • Immunology
  • Molecular Biology

Background:

  • Tripartite Motif (TRIM) proteins are E3 ubiquitin ligases regulating innate immunity.
  • TRIM25 (Efp) is involved in oestrogen receptor and innate immune signaling via RIG-I.
  • TRIM25 ubiquitinates RIG-I CARDs, initiating type I interferon production.

Purpose of the Study:

  • Determine the crystal structure of the TRIM25 B30.2 domain.
  • Identify the structural basis for TRIM25 interaction with RIG-I.
  • Characterize key residues involved in RIG-I binding.

Main Methods:

  • X-ray crystallography (1.8 Å resolution) of the TRIM25 B30.2 domain.
  • Structural comparison with other B30.2/SPRY domains.
  • Mutagenesis and functional assays.

Main Results:

  • The TRIM25 B30.2 domain adopts a canonical B30.2/SPRY fold.
  • A putative protein-binding pocket was identified within the domain.
  • Mutagenesis identified Asp488 and Trp621 as critical for RIG-I CARDs binding.

Conclusions:

  • The crystal structure provides insights into TRIM25 B30.2 domain function.
  • The identified binding pocket and key residues are essential for RIG-I recognition.
  • This structural information aids understanding of TRIM25's role in innate immunity.

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